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Metalloprotein

Spiro T G and Czernuszewicz R S 1995 Resonance Raman-spectroscopy of metalloproteins Biochemical Spectroscopy Methods Enzymol. vol 246, ed K Sauer (San Diego, CA Academic) pp 416-60... [Pg.1175]

Tissue inhibitor of metalloproteins (TIMP, from human blood plasma), Mr -30,000. [Pg.571]

Computer simulations of electron transfer proteins often entail a variety of calculation techniques electronic structure calculations, molecular mechanics, and electrostatic calculations. In this section, general considerations for calculations of metalloproteins are outlined in subsequent sections, details for studying specific redox properties are given. Quantum chemistry electronic structure calculations of the redox site are important in the calculation of the energetics of the redox site and in obtaining parameters and are discussed in Sections III.A and III.B. Both molecular mechanics and electrostatic calculations of the protein are important in understanding the outer shell energetics and are discussed in Section III.C, with a focus on molecular mechanics. [Pg.395]

METALLOPROTEINS. Metalloproteins are either metal storage forms, as in the case of ferritin, or enzymes in which the metal atom participates in a catalyti-cally important manner. We encounter many examples throughout this book of the vital metabolic functions served by metalloenzymes. [Pg.126]

Metalloproteins contain metal atoms Ferritin Iron 35... [Pg.127]

HEMOPROTEINS. These proteins are actually a subclass of metalloproteins because their prosthetic group is heme, the name given to iron protoporphyrin IX (Figure 5.15). Because heme-containing proteins enjoy so many prominent biological functions, they are considered a class by themselves. [Pg.127]

Fritz G, Heizmann CW (2004) 3D-structures of the Ca2+-and Zn2+-binding SI00 proteins. In Messerschmidt A, Bode W, Cygler M, Handbook of metalloproteins. Wiley, Chichester, pp, 529—540... [Pg.1106]

The investigation of coordinated water in paramagnetic metalloproteins through N.M.R. spectroscopy. I. Bertini, Comments Inorg. Chem., 1981,1, 227-243 (68). [Pg.47]

Redox reactions of sulphur-containing amino-acid residues in proteins and metalloproteins. [Pg.70]

Some of the critical enzymes in our cells are metalloproteins, large organic molecules made up of folded polymerized chains of amino acids that also include at least one metal atom. These metalloproteins are intensely studied by biochemists, because they control life and protect against disease. They have also been used to trace evolutionary paths. The d-block metals catalyze redox reactions, form components of membrane, muscle, skin, and bone, catalyze acid-base reactions, control the flow of energy and oxygen, and carry out nitrogen fixation. [Pg.789]

Overall practical features make the FucA and RhuA enzymes quite similar for synthetic applications. Both metalloproteins are quite robust under conditions of organic synthesis and show a very high stability in the presence of low Zn concentrations with half-lives in the range of months at room temperature. The... [Pg.286]

Sulfur-Containing Ligands in Metalloproteins and Enz mies (W. E. Newton)... [Pg.255]

Cohen lA (1980) Metal-Metal Interactions in the Metalloporphyrins, Metalloproteins and Metalloenzymes. 40 1-37... [Pg.244]

Maroney MJ, Davidson G, Allan CB, Figlar J (1998) The Structure and Function of Nickel Sites in Metalloproteins. 92 1-66... [Pg.250]

Therlen MJ, Chang J, Raphael AL, Bowler BE, Gray HB (1991) Long-Range Electron Transfer in Metalloproteins. 75 109-130... [Pg.256]

Weser U (1985) Redox Reactions of Sulphur-Containing Amino-Acid Residues in Proteins and Metalloproteins, an XPS Study. 61 145-160 Weser U (1973) Structural Aspects and Biochemical Function of Erythrocuprein. 17 1-65 Weser U, see Abolmaali B (1998) 91 91-190... [Pg.257]

The 2[4Fe-4S] and [3Fe-4S][4Fe-4S] ferredoxins are components of virtually all eubacteria and archaebacteria (3). Several comprehensive reviews dealing with these small metalloproteins have appeared (3, 8-12), but only those participating directly in the photosynthetic light reactions will be addressed here. [Pg.338]

Macrocyclic Complexes as Models for Nonporphine Metalloproteins Vickie McKee... [Pg.512]

TABLE 5 Ligand Preferences for Metals Commonly Found in Metalloproteins... [Pg.167]


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Adsorbed metalloprotein electron transfer

Adsorbed redox metalloprotein

Approaches to electrochemical ET mechanisms of multi-centre metalloproteins

Artificial metalloproteins

Azurin metalloprotein

Binding Metalloproteins

Biological Systems Metalloproteins and Related Model Compounds

Biomolecules metalloproteins

Brain, metalloproteins

Calcium-binding metalloproteins

Complexes metalloprotein

Composite metalloproteins

Coordination in Metalloproteins Structural and Electronic Aspects

Copper metalloproteins

Copper metalloproteins redox

Crystallography metalloproteins

Diiron metalloprotein

Direct metalloproteins

ESR of metalloproteins and metalloenzymes

Electrochemistry of Metalloproteins

Electrochemistry, metalloproteins

Electrochemistry, metalloproteins cytochrome

Electron between metalloproteins

Electron transfer in metalloproteins

Electron transfer metalloproteins table

Handbook on Metalloproteins

High spins metalloproteins

Hybrid metalloprotein-nanoparticle

Imaging metalloproteins

Interactions metalloproteins

Intramolecular metalloproteins

Iron metalloproteins

Macrocyclic Complexes as Models for Nonporphine Metalloproteins

Magnetic circular dichroism metalloproteins

Matrix metalloprotein

Metal Ions into Metalloproteins

Metal Metalloproteins

Metal metalloprotein reactions

Metalloprotein , resonance-enhanced

Metalloprotein Databases

Metalloprotein Voltammetry at Bare and Modified Electrodes

Metalloprotein classes

Metalloprotein donor-acceptor distances

Metalloprotein electron transfer reactions

Metalloprotein hyperfine interaction

Metalloprotein in solution

Metalloprotein interactions

Metalloprotein metal coordination site

Metalloprotein metal coordination site structures, examples

Metalloprotein metallothionein

Metalloprotein reactions, metal complex

Metalloprotein tyrosyl radicals

Metalloproteins

Metalloproteins

Metalloproteins Intramolecular electron transfer

Metalloproteins Substitution

Metalloproteins active site, model development

Metalloproteins and

Metalloproteins and Metalloenzymes

Metalloproteins and electron

Metalloproteins and electron transfer

Metalloproteins approach

Metalloproteins blue copper proteins

Metalloproteins characteristics

Metalloproteins containing

Metalloproteins cysteine

Metalloproteins electron exchange

Metalloproteins electron transfer processes

Metalloproteins electron transfer reactions

Metalloproteins electrophoresis

Metalloproteins environment

Metalloproteins geometry

Metalloproteins high-potential iron proteins

Metalloproteins histidine

Metalloproteins in solution

Metalloproteins isolation

Metalloproteins ligands

Metalloproteins metal coupling

Metalloproteins metal ligand identification

Metalloproteins metalloprotein film voltammetry

Metalloproteins model system, metalloporphyrins

Metalloproteins models

Metalloproteins nitrogenase system

Metalloproteins nonporphine

Metalloproteins paramagnetic

Metalloproteins proteins

Metalloproteins proton exchange

Metalloproteins purification

Metalloproteins redox intramolecular

Metalloproteins spin states

Metalloproteins stellacyanin

Metalloproteins substituted

Metalloproteins, NMRD profiles

Metalloproteins, active centers

Metalloproteins, active site

Metalloproteins, electron transfer

Metalloproteins, electron transfer theory

Metalloproteins, examples involved

Metalloproteins, quantum chemical calculations

Metalloproteins, quantum chemical calculations models

Metalloproteins, redox reactions

Metalloproteins, speciation analysis

Metalloproteins, tyrosyl radicals

Metalloproteins/Metalloenzymes

Metalloproteins/Metalloenzymes synthetic

Mossbauer spectroscopy metalloprotein studies

Multicenter metalloproteins

Nickel in metalloproteins

Nonheme metalloprotein

Nonporphine metalloproteins, models,

Probing Structural and Electronic Parameters in Randomly Oriented Metalloproteins by Orientation-Selective ENDOR Spectroscopy

Prosthetic group metalloprotein

Protein Crystallography for Metalloproteins

Proteins, metalloprotein redox reactions

Reactions of Metalloproteins

Reactions with Metalloproteins

Redox metalloproteins

Redox metalloproteins and oxygen

Self assembled metalloproteins

Some Examples of Mossbauer Spectroscopy Applied to Metalloprotein Studies

Some metalloproteins

Substitution in Metalloproteins

The pseudocontact shifts in paramagnetic metalloproteins

Voltammetry metalloprotein

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